Abstract
Transfection of a bovine stomach cDNA encoding for an NK2 receptor into murine fibroblasts produced a clone that exhibited specific binding of NKA, a selective NK2 agonist. In these transfected cells, NKA mediated hydrolysis of phosphatidyl-inositol (PI) with an EC50 value of 10 nM and an Emax value 7.2 times basal level. Dose response curves of IP1 accumulation by two other neurokinin agonists demonstrated a rank order of potency of NKA>SP>>senktide. This suggests that the de novo receptor expressed in these transfected cells is functionally coupled to the PI hydrolysis pathway. Stable in vitro expression of NK2 receptors in a eukaryotik cell line can provide a means of correlating the structurally defined receptor with its ligand binding properties and its functional coupling mechanisms.
Original language | English (US) |
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Pages (from-to) | PL7-PL12 |
Journal | Life Sciences |
Volume | 47 |
Issue number | 3 |
DOIs | |
State | Published - 1990 |
ASJC Scopus subject areas
- General Pharmacology, Toxicology and Pharmaceutics
- General Biochemistry, Genetics and Molecular Biology